Fractionation of Dioscorea bulbifera bulbil protein, its antioxidative potential and inhibitory effects on Carbohydrate-hydrolysing enzymes.

ODEKANYIN, Oludele Olayemi; BADMUS, Eniola Omodolapo; Akinyemi, Deborah Fehintoluwa

doi:10.30476/tips.2024.101274.1225

Fractionation of Dioscorea bulbifera bulbil protein, its antioxidative potential and inhibitory effects on Carbohydrate-hydrolysing enzymes.

Document Type : Original Article

Authors

¹ Biochemistry and Molecular Biology Department, Faculty of Science, Obafemi Awolowo University, Ile-Ife

² Biochemistry and Molecular Biology Department. Faculty of Science, Obafemi Awolowo University.

10.30476/tips.2024.101274.1225

Abstract

The study fractionated Dioscorea bulbifera bulbil protein, determined the fractions inhibitory potential on α-amylase and α-glucosidase activity, and evaluated their antioxidative activity in-vitro. Dioscorea bulbifera bulbil flesh was homogenized in Phosphate Buffer Saline (pH7.2), centrifuged at 15,000 rpm for 30 min and supernatant was subjected to ammonium sulphate fractionation. Three fractions (25%, 60% and 90%) were produced and their haemagglutinating activity, blood group and sugar specificity were determined. Ability of the fractions to inhibit α-amylase and α-glucosidase activity was investigated. Antioxidative properties were evaluated using DPPH, Nitric oxide and hydroxyl radicals scavenging assay. Their reducing power, total antioxidant capacity and ferrous chelating activity were also evaluated. Data obtained revealed the presence of lectin in the crude protein extract and 25% and 60% protein fractions. The lectin agglutinated rabbit blood erythrocyte better than human blood group erythrocyte. Protein fraction (60%) has no haemagglutinating activity towards human blood erythrocyte. Mannose completely inhibited the haemagglutinating activity. Alpha-amylase and α-glucosidase activities were inhibited by 25% and 60% protein fractions with no significant difference. But their inhibitory action was better than that of acarbose. All the free radicals tested were scavenged by the fractions to various degrees. Sixty percent protein fraction could not scavenge nitric oxide but it was a better scavenger of hydroxyl radical. No activity was recorded for 90% protein fraction. The results showed the anti-diabetic potential of the protein fractions and can be harnessed for possible development of therapeutics for the treatment of diabetes and oxidative stress associated ailments.

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